Role of membrane mimetics on biophysical EPR studies of membrane proteins

被引:4
|
作者
Sahu, Indra D. [1 ,2 ]
Lorigan, Gary A. [2 ]
机构
[1] Campbellsville Univ, Nat Sci Div, Campbellsville, KY 42718 USA
[2] Miami Univ, Dept Chem & Biochem, Oxford, OH 45056 USA
来源
基金
美国国家科学基金会;
关键词
Membrane mimetics; Detergent micelles; Lipid bilayers; Lipodisq nanoparticles; SMA copolymer; EPR spectroscopy; Structural dynamics; ELECTRON-PARAMAGNETIC-RESONANCE; BIFUNCTIONAL SPIN LABELS; BOUND ALPHA-SYNUCLEIN; DISTANCE MEASUREMENTS; LIPODISQ NANOPARTICLES; CONFORMATIONAL-CHANGES; LIPID-BILAYERS; 3-DIMENSIONAL ARCHITECTURE; SECONDARY STRUCTURE; DYNAMIC PROPERTIES;
D O I
10.1016/j.bbamem.2023.184138
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Biological membranes are essential in providing the stability of membrane proteins in a functional state. Functionally stable homogeneous sample is required for biophysical electron paramagnetic resonance (EPR) studies of membrane proteins for obtaining pertinent structural dynamics of the protein. Significant progresses have been made for the optimization of the suitable membrane environments required for biophysical EPR measurements. However, no universal membrane mimetic system is available that can solubilize all membrane proteins suitable for biophysical EPR studies while maintaining the functional integrity. Great efforts are needed to optimize the sample condition to obtain better EPR data quality of membrane proteins that can provide meaningful information on structural dynamics. In this mini-review, we will discuss important aspects of membrane mimetics for biophysical EPR measurements and current progress with some of the recent examples.
引用
收藏
页数:10
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